Characterization of the InsP6-dependent interaction between CK2 and Nopp140

Won Kyu Lee; Sang Yeop Lee; Woo Il Kim; Yoon Hwa Rho; Young Seuk Bae; Cheolju Lee; Ick Young Kim; Yeon Gyu Yu

doi:10.1016/j.bbrc.2008.09.008

Characterization of the InsP₆-dependent interaction between CK2 and Nopp140

Won Kyu Lee, Sang Yeop Lee, Woo Il Kim, Yoon Hwa Rho, Young Seuk Bae, Cheolju Lee, Ick Young Kim, Yeon Gyu Yu

Department of Life Sciences

Research output: Contribution to journal › Article › peer-review

11 Citations (Scopus)

Abstract

Nopp140, a highly phosphorylated nucleolar protein, negatively regulates CK2, a kinase essential for cell proliferation. We quantitatively analyzed the interaction between two subunits of CK2 and Nopp140 and characterized the mechanism by which InsP₆ inhibits the interaction. Nopp140 specifically binds to the catalytic subunit of CK2 (CK2α) with a dissociation constant of (K_d) of 4 nM, which interferes with the catalytic activity of CK2. The C-terminal region of Nopp140 is determined as CK2α-binding region by a yeast two-hybrid method as well as a direct measurement of the interaction between CK2α and deletion mutants of Nopp140. InsP₆ specifically binds to CK2α and disrupts the interaction between CK2α and Nopp140 with an IC₅₀ value of 25 μM, thereby attenuating the Nopp140-mediated repression of CK2 activity.

Original language	English
Pages (from-to)	439-444
Number of pages	6
Journal	Biochemical and biophysical research communications
Volume	376
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2008.09.008
Publication status	Published - 2008 Nov 14

Bibliographical note

Funding Information:
This work was supported by a grant from the Functional Proteomics Research (FPR05B2040), Ministry of Science and Technology, and by the Korea Research Foundation Grant (KRF-2006-C00137), funded by the Korean Government (MOEHRD).

Keywords

CK2
InsP
Nopp140
Protein interaction

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/j.bbrc.2008.09.008

Cite this

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title = "Characterization of the InsP6-dependent interaction between CK2 and Nopp140",

abstract = "Nopp140, a highly phosphorylated nucleolar protein, negatively regulates CK2, a kinase essential for cell proliferation. We quantitatively analyzed the interaction between two subunits of CK2 and Nopp140 and characterized the mechanism by which InsP6 inhibits the interaction. Nopp140 specifically binds to the catalytic subunit of CK2 (CK2α) with a dissociation constant of (Kd) of 4 nM, which interferes with the catalytic activity of CK2. The C-terminal region of Nopp140 is determined as CK2α-binding region by a yeast two-hybrid method as well as a direct measurement of the interaction between CK2α and deletion mutants of Nopp140. InsP6 specifically binds to CK2α and disrupts the interaction between CK2α and Nopp140 with an IC50 value of 25 μM, thereby attenuating the Nopp140-mediated repression of CK2 activity.",

keywords = "CK2, InsP, Nopp140, Protein interaction",

author = "Lee, {Won Kyu} and Lee, {Sang Yeop} and Kim, {Woo Il} and Rho, {Yoon Hwa} and Bae, {Young Seuk} and Cheolju Lee and Kim, {Ick Young} and Yu, {Yeon Gyu}",

note = "Funding Information: This work was supported by a grant from the Functional Proteomics Research (FPR05B2040), Ministry of Science and Technology, and by the Korea Research Foundation Grant (KRF-2006-C00137), funded by the Korean Government (MOEHRD). ",

year = "2008",

month = nov,

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doi = "10.1016/j.bbrc.2008.09.008",

language = "English",

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AU - Lee, Won Kyu

AU - Lee, Sang Yeop

AU - Kim, Woo Il

AU - Rho, Yoon Hwa

AU - Bae, Young Seuk

AU - Lee, Cheolju

AU - Kim, Ick Young

AU - Yu, Yeon Gyu

N1 - Funding Information: This work was supported by a grant from the Functional Proteomics Research (FPR05B2040), Ministry of Science and Technology, and by the Korea Research Foundation Grant (KRF-2006-C00137), funded by the Korean Government (MOEHRD).

PY - 2008/11/14

Y1 - 2008/11/14

N2 - Nopp140, a highly phosphorylated nucleolar protein, negatively regulates CK2, a kinase essential for cell proliferation. We quantitatively analyzed the interaction between two subunits of CK2 and Nopp140 and characterized the mechanism by which InsP6 inhibits the interaction. Nopp140 specifically binds to the catalytic subunit of CK2 (CK2α) with a dissociation constant of (Kd) of 4 nM, which interferes with the catalytic activity of CK2. The C-terminal region of Nopp140 is determined as CK2α-binding region by a yeast two-hybrid method as well as a direct measurement of the interaction between CK2α and deletion mutants of Nopp140. InsP6 specifically binds to CK2α and disrupts the interaction between CK2α and Nopp140 with an IC50 value of 25 μM, thereby attenuating the Nopp140-mediated repression of CK2 activity.

AB - Nopp140, a highly phosphorylated nucleolar protein, negatively regulates CK2, a kinase essential for cell proliferation. We quantitatively analyzed the interaction between two subunits of CK2 and Nopp140 and characterized the mechanism by which InsP6 inhibits the interaction. Nopp140 specifically binds to the catalytic subunit of CK2 (CK2α) with a dissociation constant of (Kd) of 4 nM, which interferes with the catalytic activity of CK2. The C-terminal region of Nopp140 is determined as CK2α-binding region by a yeast two-hybrid method as well as a direct measurement of the interaction between CK2α and deletion mutants of Nopp140. InsP6 specifically binds to CK2α and disrupts the interaction between CK2α and Nopp140 with an IC50 value of 25 μM, thereby attenuating the Nopp140-mediated repression of CK2 activity.

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